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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization.

Heat shock induces in cells the development of a transient state of thermotolerance thought to result from the induction of heat shock proteins. To assess directly whether a transient overexpression of one of these proteins, HSP27, can contribute to increased cellular resistance, mouse NIH/3T3 cells were cotransfected with a plasmid containing the Chinese hamster HSP27 gene under the control of the metallothionein promoter and a plasmid containing the neo gene. Stable transfectant cell lines were selected for resistance to the antibiotic G418. Analyses of several stable transfectant cell lines indicated that expression of Chinese hamster HSP27 could be selectively induced by exposure to 3 microM CdCl2, a concentration that had no effect on the induction of the endogenous heat shock proteins (HSP). In clone 15, the level of HSP27 increased steadily during the first day of exposure to CdCl2, from a concentration of 1 microgram/mg of total protein to 7 micrograms/mg. After withdrawal of CdCl2, the level of HSP27 returned to normal within the next 5 days. Accumulation of the Chinese hamster HSP27 was accompanied by a progressive development of thermoresistance that attained a level approaching heat shock-induced thermotolerance. After CdCl2 removal, thermal resistance and HSP27 decayed in a coordinated manner. In control cells transfected with the neo gene only, increased thermoresistance was not induced by 3 microM CdCl2; in these cells, an exposure to 20 microM CdCl2 was required to induce a level of thermoresistance comparable to that induced by 3 microM CdCl2 in clone 15. Elevated expression of HSP27 was accompanied by an increased stability of stress fibers during hyperthermia. The protein also partially prevented actin depolymerization during acute exposure to cytochalasin D and reduced cytotoxicity and growth inhibition of chronic exposures to the drug. The results indicated that accumulation of HSP27, as it occurs after a mild heat shock or other inducing treatments, is sufficient for acquisition of thermotolerance that may result in part from a stabilization of actin filaments.[1]


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